Research workbench
PLMKR1-ketoreductase from the first module of phoslactomycin biosynthesis in streptomyces sp. HK803
Analyse PLMKR1-ketoreductase from the first module of phoslactomycin biosynthesis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HXY
- Type
- protein
- Length
- 855 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PLM1
- UniProt
- Q6V1M8
- Ligands
- NDP, ACA
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PLM1 | protein | 425 | 39% helix, 21% strand | Q6V1M8 |
| B | PLM1 | protein | 430 | 39% helix, 22% strand | Q6V1M8 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ACA · 6-aminohexanoic acid · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.76 | 0.83 | 65 | NDP, ACA |
| 2 | 552 | 0.72 | 0.81 | 66 | NDP |
| 3 | 805 | 0.68 | 0.75 | 77 | empty |
| 4 | 315 | 0.67 | 0.82 | 51 | empty |
| 5 | 314 | 0.66 | 0.81 | 46 | empty |
Interfaces
1 interface between chains.
- A–B · 631 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4HXY · PlmKR1-Ketoreductase from the first module of phoslactomycin biosynthesis in Streptomyces… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q6V1M8
- Elsewhere: RCSB PDB 4HXY · PDBe 4HXY · UniProt Q6V1M8
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